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14-3-3 Interaction with Histone H3 Involves a Dual Modification Pattern of Phosphoacetylation

Wendy Walter,^1, David Clynes,^2, Yong Tang,¹ Ronen Marmorstein,¹ Jane Mellor,^2* and Shelley L. Berger^1*

Gene Expression and Regulation Program, The Wistar Institute, Philadelphia, Pennsylvania 19104,¹ Division of Molecular Genetics, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom²

Received 13 August 2007/ Returned for modification 8 September 2007/ Accepted 30 January 2008

Histone modifications occur in precise patterns and are proposed to signal the recruitment of effector molecules that profoundly impact chromatin structure, gene regulation, and cell cycle events. The linked modifications serine 10 phosphorylation and lysine 14 acetylation on histone H3 (H3S10phK14ac), modifications conserved from Saccharomyces cerevisiae to humans, are crucial for transcriptional activation of many genes. However, the mechanism of H3S10phK14ac involvement in these processes is unclear. To shed light on the role of this dual modification, we utilized H3 peptide affinity assays to identify H3S10phK14ac-interacting proteins. We found that the interaction of the known phospho-binding 14-3-3 proteins with H3 is dependent on the presence of both of these marks, not just phosphorylation alone. This is true of mammalian 14-3-3 proteins as well as the yeast homologues Bmh1 and Bmh2. The importance of acetylation in this interaction is also seen in vivo, where K14 acetylation is required for optimal Bmh1 recruitment to the GAL1 promoter during transcriptional activation.

Published ahead of print on 11 February 2008.

These two authors contributed equally.